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Entry version 140 (08 May 2019)
Sequence version 2 (05 Jul 2004)
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Protein

Protein adenylyltransferase FICD

Gene

FICD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (PubMed:25601083). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By similarity). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (PubMed:19362538, PubMed:25601083).By similarity1 Publication3 Publications

Caution

Was initially thought to mediate AMPylation of HSPA5/BiP at 'Ser-365' and 'Thr-366' in vitro, leading to activate HSPA5/BiP (PubMed:25601083). However, it was later shown that it mediates AMPylation of HSPA5/BiP at 'Thr-518', leading to inactivate HSPA5/BiP.By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Divalent metal cation. Prefers Mn2+ over Mg2+.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The side chain of Glu-234 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place. In response to endoplasmic reticulum stress, mediates de-AMPylase activity (By similarity). Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-234 binds ATP and competes with ATP-binding at Arg-374, thereby preventing adenylyltransferase activity (PubMed:22266942, PubMed:25435325). In unstressed cells, disengagement of Glu-234 promotes adenylyltransferase activity (By similarity). Activation dissociates ATP-binding from Glu-234, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain (PubMed:22266942, PubMed:25435325).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei234ATP; via amide nitrogenCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei234Important for autoinhibition of adenylyltransferase activity2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei3631 Publication1
Binding sitei407ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi316 – 319ATPCombined sources1 Publication4
Nucleotide bindingi367 – 374ATPCombined sources1 Publication8
Nucleotide bindingi399 – 400ATPCombined sources1 Publication2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Nucleotidyltransferase, Transferase
Biological processUnfolded protein response
LigandATP-binding, Magnesium, Manganese, Nucleotide-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protein adenylyltransferase FICDCurated (EC:2.7.7.n13 Publications)
Alternative name(s):
AMPylator FICDCurated
De-AMPylase FICDBy similarity (EC:3.1.4.-By similarity)
FIC domain-containing protein1 Publication
Huntingtin yeast partner E2 Publications
Huntingtin-interacting protein 13
Short name:
HIP-13
Huntingtin-interacting protein E2 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FICDImported
Synonyms:HIP13, HYPE2 Publications
ORF Names:UNQ3041/PRO9857
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:18416 FICD

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9BVA6

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 23Cytoplasmic1 PublicationAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei24 – 44Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini45 – 458Lumenal1 PublicationAdd BLAST414

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi76 – 77TS → AA: Does not affect auto-AMPylation. 1 Publication2
Mutagenesisi79 – 80ST → AA: Decreased AMPylation. 1 Publication2
Mutagenesisi168T → A: Does not affect level of auto-AMPylation. 1 Publication1
Mutagenesisi170S → A: Does not affect level of auto-AMPylation. 1 Publication1
Mutagenesisi172Y → F: Does not affect level of auto-AMPylation. 1 Publication1
Mutagenesisi183T → A: Decreased AMPylation. 1 Publication1
Mutagenesisi234E → G: Promotes adenylyltransferase activity. 3 Publications1
Mutagenesisi258L → D: Abolishes homodimerization. 1 Publication1
Mutagenesisi275N → Q: Strongly decreased N-glycosylation. Abolished N-glycosylation; when associated with Q-446. 1 Publication1
Mutagenesisi363H → A: Abolishes adenylyltransferase activity. 2 Publications1
Mutagenesisi446N → Q: Slightly decreased N-glycosylation. Abolished N-glycosylation; when associated with Q-275. 1 Publication1

Organism-specific databases

Open Targets

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OpenTargetsi
ENSG00000198855

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA162388517

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
FICD

Domain mapping of disease mutations (DMDM)

More...
DMDMi
74761284

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003173011 – 458Protein adenylyltransferase FICDAdd BLAST458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei79O-AMP-serine; by autocatalysis1 Publication1
Modified residuei80O-AMP-threonine; by autocatalysis1 Publication1
Modified residuei183O-AMP-threonine; by autocatalysis1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi275N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1
Glycosylationi446N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Auto-AMPylated in vitro; it is unclear whether auto-AMPylation is relevant in vivo.2 Publications
N-glycosylated; predominantly glycosylated at Asn-275.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9BVA6

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9BVA6

PeptideAtlas

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PeptideAtlasi
Q9BVA6

PRoteomics IDEntifications database

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PRIDEi
Q9BVA6

ProteomicsDB human proteome resource

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ProteomicsDBi
79191

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9BVA6

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9BVA6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in response to activation of unfolded protein response (UPR).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000198855 Expressed in 180 organ(s), highest expression level in pigmented layer of retina

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9BVA6 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9BVA6 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA021390
HPA071134

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:25435325). Interacts with HD (PubMed:9700202).2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-3907198,EBI-3907198

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
116324, 3 interactors

Database of interacting proteins

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DIPi
DIP-44884N

Protein interaction database and analysis system

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IntActi
Q9BVA6, 3 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000446479

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1458
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9BVA6

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati106 – 139TPR 1Add BLAST34
Repeati140 – 173TPR 2Add BLAST34
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini285 – 420FidoPROSITE-ProRule annotationAdd BLAST136

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi230 – 235Inhibitory (S/T)XXXE(G/N) motif1 Publication6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The fido domain mediates the adenylyltransferase activity.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the fic family.Curated

Keywords - Domaini

Repeat, Signal-anchor, TPR repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3824 Eukaryota
COG3177 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000008873

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000008059

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9BVA6

Identification of Orthologs from Complete Genome Data

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OMAi
NYAALAH

Database of Orthologous Groups

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OrthoDBi
1057856at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9BVA6

TreeFam database of animal gene trees

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TreeFami
TF314692

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.3290.10, 1 hit
1.25.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003812 Fido
IPR036597 Fido-like_dom_sf
IPR040198 Fido_containing
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat

The PANTHER Classification System

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PANTHERi
PTHR13504 PTHR13504, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02661 Fic, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF140931 SSF140931, 1 hit
SSF48452 SSF48452, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51459 FIDO, 1 hit
PS50005 TPR, 2 hits
PS50293 TPR_REGION, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q9BVA6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMLIPMASVM AVTEPKWVSV WSRFLWVTLL SMVLGSLLAL LLPLGAVEEQ
60 70 80 90 100
CLAVLKGLYL LRSKPDRAQH AATKCTSPST ELSITSRGAT LLVAKTKASP
110 120 130 140 150
AGKLEARAAL NQALEMKRQG KREKAQKLFM HALKMDPDFV DALTEFGIFS
160 170 180 190 200
EEDKDIIQAD YLYTRALTIS PYHEKALVNR DRTLPLVEEI DQRYFSIIDS
210 220 230 240 250
KVKKVMSIPK GNSALRRVME ETYYHHIYHT VAIEGNTLTL SEIRHILETR
260 270 280 290 300
YAVPGKSLEE QNEVIGMHAA MKYINTTLVS RIGSVTISDV LEIHRRVLGY
310 320 330 340 350
VDPVEAGRFR TTQVLVGHHI PPHPQDVEKQ MQEFVQWLNS EEAMNLHPVE
360 370 380 390 400
FAALAHYKLV YIHPFIDGNG RTSRLLMNLI LMQAGYPPIT IRKEQRSDYY
410 420 430 440 450
HVLEAANEGD VRPFIRFIAK CTETTLDTLL FATTEYSVAL PEAQPNHSGF

KETLPVKP
Length:458
Mass (Da):51,778
Last modified:July 5, 2004 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8393EAA46D61C48E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3KP49J3KP49_HUMAN
Protein adenylyltransferase FICD
FICD
180Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VZ74F8VZ74_HUMAN
Protein adenylyltransferase FICD
FICD
139Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YIR6H0YIR6_HUMAN
Protein adenylyltransferase FICD
FICD
56Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AY358992 mRNA Translation: AAQ89351.1
CH471054 Genomic DNA Translation: EAW97813.1
BC001342 mRNA Translation: AAH01342.2
AF049611 mRNA Translation: AAC26847.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS9116.1

NCBI Reference Sequences

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RefSeqi
NP_009007.2, NM_007076.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000552695; ENSP00000446479; ENSG00000198855

Database of genes from NCBI RefSeq genomes

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GeneIDi
11153

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:11153

UCSC genome browser

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UCSCi
uc001tmx.2 human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358992 mRNA Translation: AAQ89351.1
CH471054 Genomic DNA Translation: EAW97813.1
BC001342 mRNA Translation: AAH01342.2
AF049611 mRNA Translation: AAC26847.1
CCDSiCCDS9116.1
RefSeqiNP_009007.2, NM_007076.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4U04X-ray2.48A/B102-445[»]
4U07X-ray2.64A/B102-445[»]
4U0SX-ray2.49A/B102-445[»]
4U0UX-ray2.98A/B102-445[»]
4U0ZX-ray2.95A/B/C/D/E/F/G/H102-445[»]
SMRiQ9BVA6
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116324, 3 interactors
DIPiDIP-44884N
IntActiQ9BVA6, 3 interactors
STRINGi9606.ENSP00000446479

PTM databases

iPTMnetiQ9BVA6
PhosphoSitePlusiQ9BVA6

Polymorphism and mutation databases

BioMutaiFICD
DMDMi74761284

Proteomic databases

jPOSTiQ9BVA6
PaxDbiQ9BVA6
PeptideAtlasiQ9BVA6
PRIDEiQ9BVA6
ProteomicsDBi79191

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
11153
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000552695; ENSP00000446479; ENSG00000198855
GeneIDi11153
KEGGihsa:11153
UCSCiuc001tmx.2 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
11153

GeneCards: human genes, protein and diseases

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GeneCardsi
FICD

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0010965
HGNCiHGNC:18416 FICD
HPAiHPA021390
HPA071134
neXtProtiNX_Q9BVA6
OpenTargetsiENSG00000198855
PharmGKBiPA162388517

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3824 Eukaryota
COG3177 LUCA
GeneTreeiENSGT00390000008873
HOGENOMiHOG000008059
InParanoidiQ9BVA6
OMAiNYAALAH
OrthoDBi1057856at2759
PhylomeDBiQ9BVA6
TreeFamiTF314692

Miscellaneous databases

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
11153

Protein Ontology

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PROi
PR:Q9BVA6

Gene expression databases

BgeeiENSG00000198855 Expressed in 180 organ(s), highest expression level in pigmented layer of retina
ExpressionAtlasiQ9BVA6 baseline and differential
GenevisibleiQ9BVA6 HS

Family and domain databases

Gene3Di1.10.3290.10, 1 hit
1.25.40.10, 1 hit
InterProiView protein in InterPro
IPR003812 Fido
IPR036597 Fido-like_dom_sf
IPR040198 Fido_containing
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_repeat
PANTHERiPTHR13504 PTHR13504, 1 hit
PfamiView protein in Pfam
PF02661 Fic, 1 hit
SUPFAMiSSF140931 SSF140931, 1 hit
SSF48452 SSF48452, 1 hit
PROSITEiView protein in PROSITE
PS51459 FIDO, 1 hit
PS50005 TPR, 2 hits
PS50293 TPR_REGION, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFICD_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9BVA6
Secondary accession number(s): O75406
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 5, 2004
Last modified: May 8, 2019
This is version 140 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
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